Abstract
Sec14 is a phosphatidylinositol (PI) transfer protein that functions in transport from the Golgi apparatus and regulation of lipid metabolism in Saccharomyces cerevisiae. This protein is the namesake of the Sec14 family of proteins that includes relatives in a wide variety of eukaryotic organisms. Structural models of the Sec14 lipid binding domain predicted it would have increased selectivity for particular phosphorylated PI derivatives, such as PI5P. Lipid binding assays for Sec14 confirmed this previously unreported preference, which has also been observed for the homologous Sec14 protein Patellin from Arabidopsis thaliana. We also have extended our computational modeling to Sec14 proteins from the moss Physcomitrella patens in order to predict their lipid binding profiles. Ongoing work is aimed at experimentally confirming these computational predictions. A robust computational model for Sec14 lipid binding would simplify functional predictions, providing insight into the physiological function for these proteins.
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